5fit Summary



The structure was published by Lima, C.D., Klein, M.G., and Hendrickson, W.A., in 1997 in a paper entitled "Structure-based analysis of catalysis and substrate definition in the HIT protein family." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1997.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of FRAGILE HISTIDINE TRIAD PROTEIN. This molecule has the UniProt identifier P49789 (FHIT_HUMAN)search. The sample contained 147 residues which is 100% of the natural sequence. Out of 147 residues 126 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A FRAGILE HISTIDINE TRIAD PROTEIN P49789 (1-147) (FHIT_HUMAN)search Homo sapienssearch 100% 147 85%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P49789 (1 - 147) FRAGILE HISTIDINE TRIAD PROTEIN Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P49789) HIT (HINT, histidine triad) family of protein kinase-interacting proteinssearch HIT family, subunit Asearch PF01230: HIT domainsearch

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A (P49789) mitochondrionsearch cytoplasmsearch cytosolsearch extracellular vesicular exosomesearch nucleussearch purine nucleotide metabolic processsearch apoptotic processsearch DNA replicationsearch transcription, DNA-templatedsearch nucleotide metabolic processsearch regulation of transcription, DNA-templatedsearch negative regulation of proteasomal ubiquitin-dependent protein catabolic processsearch intrinsic apoptotic signaling pathway by p53 class mediatorsearch catalytic activitysearch hydrolase activitysearch identical protein bindingsearch nucleotide bindingsearch bis(5'-adenosyl)-triphosphatase activitysearch protein bindingsearch ubiquitin protein ligase bindingsearch

Chain InterPro annotation
A Histidine triad (HIT) proteinsearch HIT-like domainsearch Histidine triad, conserved sitesearch